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Conserved domains on  [gi|755532339|ref|XP_011241342|]
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cAMP-regulated phosphoprotein 21 isoform X8 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 1.11e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100071  Cd Length: 63  Bit Score: 100.37  E-value: 1.11e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532339 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
PRK10927 super family cl35972
cell division protein FtsN;
558-709 4.58e-04

cell division protein FtsN;


The actual alignment was detected with superfamily member PRK10927:

Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 43.13  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339 558 SRQSSGDTPEPPSG---TVYPASLLPQTAQPQSYVITSAGQQ---LSTGGFSDSGPPISQQVLQAPPSPQGFVQQPPPAQ 631
Cdd:PRK10927  91 SRQPGVRAPTEPSAggeVKTPEQLTPEQRQLLEQMQADMRQQptqLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQ 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532339 632 MSVYYYPSGQYPTSTSQQyrplasvQYSAQRSQQIPQTTQQAGYQPVLsgqqgfqgmmgvQQSAHSQGVMSSQQGAPV 709
Cdd:PRK10927 171 QSRTTEQSWQQQTRTSQA-------APVQAQPRQSKPASTQQPYQDLL------------QTPAHTTAQSKPQQAAPV 229
PHA03247 super family cl33720
large tegument protein UL36; Provisional
387-734 7.51e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  387 SRTHPQSTALTSSVAAGSPGCMAYSENGMGGQVPPSSTSYILLPLESATGIPPGSillnphtgqpfVNPDGTPAIYNPPG 466
Cdd:PHA03247 2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----------PARPARPPTTAGPP 2767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  467 SQQTLRGTVGGQPQQPPQQQPSPQPQQQVQASQPQMAGPlVTQSVQSLQPSSQSVQYPAVSFPPqhllpmsPTQHFPLRE 546
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD-PPAAVLAPAAALPPAASPAGPLPP-------PTSAQPTAP 2839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  547 ELAAQFSQlsmsrqssgdTPEPPSGTVYPASLLPQTAQPQSYVITSAgqqlstggfSDSGPPISQQVLQAPPSPQGFVQQ 626
Cdd:PHA03247 2840 PPPPGPPP----------PSLPLGGSVAPGGDVRRRPPSRSPAAKPA---------APARPPVRRLARPAVSRSTESFAL 2900
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  627 PPPAQmsvyyypsgQYPTSTSQQYRPLASVQYSAQRSQQiPQTTQQAGYQPVLSGQQGFQGmmgvqQSAHSQGVMSSQQG 706
Cdd:PHA03247 2901 PPDQP---------ERPPQPQAPPPPQPQPQPPPPPQPQ-PPPPPPPRPQPPLAPTTDPAG-----AGEPSGAVPQPWLG 2965
                         330       340
                  ....*....|....*....|....*...
gi 755532339  707 APVHGvmvsyptmsSYQVPMTQGSQAVP 734
Cdd:PHA03247 2966 ALVPG---------RVAVPRFRVPQPAP 2984
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 1.11e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 100.37  E-value: 1.11e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532339 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 3.13e-13

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 65.40  E-value: 3.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339   146 IDLHGFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteristic spacing of the most ...
166-222 2.19e-12

R3H domain; The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 426259  Cd Length: 60  Bit Score: 62.48  E-value: 2.19e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755532339  166 LLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   3 LEKLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVITK 60
PRK10927 PRK10927
cell division protein FtsN;
558-709 4.58e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 43.13  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339 558 SRQSSGDTPEPPSG---TVYPASLLPQTAQPQSYVITSAGQQ---LSTGGFSDSGPPISQQVLQAPPSPQGFVQQPPPAQ 631
Cdd:PRK10927  91 SRQPGVRAPTEPSAggeVKTPEQLTPEQRQLLEQMQADMRQQptqLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQ 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532339 632 MSVYYYPSGQYPTSTSQQyrplasvQYSAQRSQQIPQTTQQAGYQPVLsgqqgfqgmmgvQQSAHSQGVMSSQQGAPV 709
Cdd:PRK10927 171 QSRTTEQSWQQQTRTSQA-------APVQAQPRQSKPASTQQPYQDLL------------QTPAHTTAQSKPQQAAPV 229
PHA03247 PHA03247
large tegument protein UL36; Provisional
387-734 7.51e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  387 SRTHPQSTALTSSVAAGSPGCMAYSENGMGGQVPPSSTSYILLPLESATGIPPGSillnphtgqpfVNPDGTPAIYNPPG 466
Cdd:PHA03247 2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----------PARPARPPTTAGPP 2767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  467 SQQTLRGTVGGQPQQPPQQQPSPQPQQQVQASQPQMAGPlVTQSVQSLQPSSQSVQYPAVSFPPqhllpmsPTQHFPLRE 546
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD-PPAAVLAPAAALPPAASPAGPLPP-------PTSAQPTAP 2839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  547 ELAAQFSQlsmsrqssgdTPEPPSGTVYPASLLPQTAQPQSYVITSAgqqlstggfSDSGPPISQQVLQAPPSPQGFVQQ 626
Cdd:PHA03247 2840 PPPPGPPP----------PSLPLGGSVAPGGDVRRRPPSRSPAAKPA---------APARPPVRRLARPAVSRSTESFAL 2900
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  627 PPPAQmsvyyypsgQYPTSTSQQYRPLASVQYSAQRSQQiPQTTQQAGYQPVLSGQQGFQGmmgvqQSAHSQGVMSSQQG 706
Cdd:PHA03247 2901 PPDQP---------ERPPQPQAPPPPQPQPQPPPPPQPQ-PPPPPPPRPQPPLAPTTDPAG-----AGEPSGAVPQPWLG 2965
                         330       340
                  ....*....|....*....|....*...
gi 755532339  707 APVHGvmvsyptmsSYQVPMTQGSQAVP 734
Cdd:PHA03247 2966 ALVPG---------RVAVPRFRVPQPAP 2984
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
545-682 1.10e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  545 REELAAQFSQLSM-SRQSSGDTPEPPSgtvYPASLLPQTAQPQSYvitsAGQQLstgGFSDSGPPISQQVLQAPPSPQGF 623
Cdd:TIGR01628 368 RAHLQDQFMQLQPrMRQLPMGSPMGGA---MGQPPYYGQGPQQQF----NGQPL---GWPRMSMMPTPMGPGGPLRPNGL 437
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755532339  624 VQQPPPAQMSVYYYPSGQYPTSTSQQYRPLASVQYSAQRSQQIPQTTQQAGYQPVLSGQ 682
Cdd:TIGR01628 438 APMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 1.11e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 100.37  E-value: 1.11e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532339 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642    1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 3.13e-13

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 65.40  E-value: 3.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339   146 IDLHGFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteristic spacing of the most ...
166-222 2.19e-12

R3H domain; The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 426259  Cd Length: 60  Bit Score: 62.48  E-value: 2.19e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755532339  166 LLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   3 LEKLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVITK 60
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
166-222 3.29e-12

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 61.86  E-value: 3.29e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755532339 166 LLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINK 222
Cdd:cd02325    1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
PRK10927 PRK10927
cell division protein FtsN;
558-709 4.58e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 43.13  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339 558 SRQSSGDTPEPPSG---TVYPASLLPQTAQPQSYVITSAGQQ---LSTGGFSDSGPPISQQVLQAPPSPQGFVQQPPPAQ 631
Cdd:PRK10927  91 SRQPGVRAPTEPSAggeVKTPEQLTPEQRQLLEQMQADMRQQptqLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQ 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532339 632 MSVYYYPSGQYPTSTSQQyrplasvQYSAQRSQQIPQTTQQAGYQPVLsgqqgfqgmmgvQQSAHSQGVMSSQQGAPV 709
Cdd:PRK10927 171 QSRTTEQSWQQQTRTSQA-------APVQAQPRQSKPASTQQPYQDLL------------QTPAHTTAQSKPQQAAPV 229
PHA03247 PHA03247
large tegument protein UL36; Provisional
387-734 7.51e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  387 SRTHPQSTALTSSVAAGSPGCMAYSENGMGGQVPPSSTSYILLPLESATGIPPGSillnphtgqpfVNPDGTPAIYNPPG 466
Cdd:PHA03247 2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----------PARPARPPTTAGPP 2767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  467 SQQTLRGTVGGQPQQPPQQQPSPQPQQQVQASQPQMAGPlVTQSVQSLQPSSQSVQYPAVSFPPqhllpmsPTQHFPLRE 546
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD-PPAAVLAPAAALPPAASPAGPLPP-------PTSAQPTAP 2839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  547 ELAAQFSQlsmsrqssgdTPEPPSGTVYPASLLPQTAQPQSYVITSAgqqlstggfSDSGPPISQQVLQAPPSPQGFVQQ 626
Cdd:PHA03247 2840 PPPPGPPP----------PSLPLGGSVAPGGDVRRRPPSRSPAAKPA---------APARPPVRRLARPAVSRSTESFAL 2900
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  627 PPPAQmsvyyypsgQYPTSTSQQYRPLASVQYSAQRSQQiPQTTQQAGYQPVLSGQQGFQGmmgvqQSAHSQGVMSSQQG 706
Cdd:PHA03247 2901 PPDQP---------ERPPQPQAPPPPQPQPQPPPPPQPQ-PPPPPPPRPQPPLAPTTDPAG-----AGEPSGAVPQPWLG 2965
                         330       340
                  ....*....|....*....|....*...
gi 755532339  707 APVHGvmvsyptmsSYQVPMTQGSQAVP 734
Cdd:PHA03247 2966 ALVPG---------RVAVPRFRVPQPAP 2984
PRK10263 PRK10263
DNA translocase FtsK; Provisional
545-767 1.02e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  545 REELAAQFSQLSMSR---QSSGDTPEPP--SGTVYPASLLPQTAQPQsyvitsagQQLSTGGFSDSGPPISQQVLQAPPS 619
Cdd:PRK10263  661 QDELARQFAQTQQQRygeQYQHDVPVNAedADAAAEAELARQFAQTQ--------QQRYSGEQPAGANPFSLDDFEFSPM 732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  620 pQGFVQQPPPAQMsvyyYPSGQYPTSTSQQyRPLASVQYSAQRSQQIPQTTQQAGYQPVLSGQQGFQGMMGVQQSAHSQG 699
Cdd:PRK10263  733 -KALLDDGPHEPL----FTPIVEPVQQPQQ-PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 806
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  700 VMSSQQGAPvhgvmvsyptmsSYQVPMtqgSQAVPQQTYQPPIMLPSQAGQGSL----------------PATGMPVYCN 763
Cdd:PRK10263  807 PQQPVAPQP------------QYQQPQ---QPVAPQPQYQQPQQPVAPQPQDTLlhpllmrngdsrplhkPTTPLPSLDL 871

                  ....
gi 755532339  764 VTPP 767
Cdd:PRK10263  872 LTPP 875
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
545-682 1.10e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  545 REELAAQFSQLSM-SRQSSGDTPEPPSgtvYPASLLPQTAQPQSYvitsAGQQLstgGFSDSGPPISQQVLQAPPSPQGF 623
Cdd:TIGR01628 368 RAHLQDQFMQLQPrMRQLPMGSPMGGA---MGQPPYYGQGPQQQF----NGQPL---GWPRMSMMPTPMGPGGPLRPNGL 437
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755532339  624 VQQPPPAQMSVYYYPSGQYPTSTSQQYRPLASVQYSAQRSQQIPQTTQQAGYQPVLSGQ 682
Cdd:TIGR01628 438 APMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
PRK10263 PRK10263
DNA translocase FtsK; Provisional
531-727 1.74e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  531 QHLLPMSPTQHFPLRE-ELAAQFSQLSMSRQSSgdtpEPPSGTvYPASLLPQTAQPQSYVITSAGQQLStggFSDSGPPI 609
Cdd:PRK10263  681 QHDVPVNAEDADAAAEaELARQFAQTQQQRYSG----EQPAGA-NPFSLDDFEFSPMKALLDDGPHEPL---FTPIVEPV 752
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  610 SQQVLQAPPSPQGFVQQPPPAQMSVYYYPsgQYPTSTSQQYR-PLASVQYSAQRSQ-QIPQTTQQAGYQPvlsgQQGFQG 687
Cdd:PRK10263  753 QQPQQPVAPQQQYQQPQQPVAPQPQYQQP--QQPVAPQPQYQqPQQPVAPQPQYQQpQQPVAPQPQYQQP----QQPVAP 826
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 755532339  688 MMGVQQsaHSQGVMSSQQGAPVHGVMVSYPTMSSYQVPMT 727
Cdd:PRK10263  827 QPQYQQ--PQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTT 864
R3H_sperm-antigen cd02636
R3H domain of a group of metazoan proteins that is related to the sperm-associated antigen 7. ...
168-207 2.43e-03

R3H domain of a group of metazoan proteins that is related to the sperm-associated antigen 7. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100065  Cd Length: 61  Bit Score: 36.92  E-value: 2.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755532339 168 KMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGL 207
Cdd:cd02636    3 SMEKEVSKFIKDSVRTREKFQPMDKVERSIVHDVAEVAGL 42
PRK10263 PRK10263
DNA translocase FtsK; Provisional
573-761 3.62e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  573 VYPASLLPQTAQPQSYVITSAGQQLSTGGFSDSGPPISQQVLQapPSPQGFVQQPPPAQMSVYYYPSGQYPTSTSQQYRP 652
Cdd:PRK10263  332 SWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIA--PAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYA 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532339  653 LASVQYSAQrsQQIPQTTQQAGYQPVLSGQqgfqgmmgVQQSAHSQGVMSSQQGaPVHGVMVSYPTMSSYQVPMTQGSQA 732
Cdd:PRK10263  410 PAAEQPAQQ--PYYAPAPEQPAQQPYYAPA--------PEQPVAGNAWQAEEQQ-STFAPQSTYQTEQTYQQPAAQEPLY 478
                         170       180
                  ....*....|....*....|....*....
gi 755532339  733 VPQQTYQPPIMLPSQAGQGSLPATGMPVY 761
Cdd:PRK10263  479 QQPQPVEQQPVVEPEPVVEETKPARPPLY 507
R3H_Smubp-2_like cd02641
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ...
176-220 4.47e-03

R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100070  Cd Length: 60  Bit Score: 36.18  E-value: 4.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755532339 176 FIADSNNHYKKFP-QMSSYQRMLVHRVAAYFGLDHNVDQTGKSVII 220
Cdd:cd02641   11 FMKDPKATELEFPpTLSSHDRLLVHELAEELGLRHESTGEGSDRVI 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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